Title

Crystallization and Preliminary X-ray Diffraction Studies on the DNA-Binding Domain of the Multidrug Transporter Activation Protein (MtaN) from Bacillus subtilis

Authors

M. H. GodseyFollow
N. N. Baranova
A. A. Neyfakh
R. G. Brennan

Document Type

Article

Publication Date

11-1-2000

Abstract

The N-terminal DNA-binding domain of the multidrug transporter activation protein (MtaN) was crystallized by the hanging-drop vapour-diffusion method using lithium chloride as a precipitant. The crystals are orthorhombic and belong to the space group I2₁2₁2₁, with unit-cell parameters a = 49.4, b = 67.8, c = 115.0 Å. Diffraction data have been collected at 100 K to 2.75 Å resolution at a synchrotron-radiation source.

Comments

Publication Information.

Godsey, M. H., Baranova, N. N., Neyfakh, A. A., & Brennan, R. G. (2000). Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the multidrug transporter activation protein (MtaN) from Bacillus subtilis. Acta Crystallographica, Section D, Biological Crystallography, 56(Pt. 11), 1456-1458. doi:10.1107/S0907444900010295

doi:10.1107/S0907444900010295

Published In

Acta Crystallographica, Section D, Biological Crystallography

Recommended Citation

Godsey, M. H.; Baranova, N. N.; Neyfakh, A. A.; and Brennan, R. G., "Crystallization and Preliminary X-ray Diffraction Studies on the DNA-Binding Domain of the Multidrug Transporter Activation Protein (MtaN) from Bacillus subtilis" (2000). CUP Faculty Research. 129.
https://digitalcommons.csp.edu/cup_commons_faculty/129

Source

CU Commons -- Math and Science Department Faculty Research